TRM14_METJA
ID TRM14_METJA Reviewed; 381 AA.
AC Q57880;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=tRNA (guanine(6)-N2)-methyltransferase {ECO:0000305};
DE EC=2.1.1.256 {ECO:0000269|PubMed:21693558};
DE AltName: Full=tRNA m2G6-methyltransferase {ECO:0000305};
GN Name=trm14 {ECO:0000303|PubMed:21693558}; OrderedLocusNames=MJ0438;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND GENE NAME.
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=21693558; DOI=10.1093/nar/gkr475;
RA Menezes S., Gaston K.W., Krivos K.L., Apolinario E.E., Reich N.O.,
RA Sowers K.R., Limbach P.A., Perona J.J.;
RT "Formation of m2G6 in Methanocaldococcus jannaschii tRNA catalyzed by the
RT novel methyltransferase Trm14.";
RL Nucleic Acids Res. 39:7641-7655(2011).
CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that
CC catalyzes the methylation of the guanosine nucleotide at position 6
CC (m2G6) in tRNA(Cys). {ECO:0000269|PubMed:21693558}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(6) in tRNA + S-adenosyl-L-methionine = H(+) + N(2)-
CC methylguanosine(6) in tRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:51116, Rhea:RHEA-COMP:12888, Rhea:RHEA-COMP:12889,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:74269, ChEBI:CHEBI:74481; EC=2.1.1.256;
CC Evidence={ECO:0000269|PubMed:21693558};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC {ECO:0000305}.
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DR EMBL; L77117; AAB98426.1; -; Genomic_DNA.
DR PIR; F64354; F64354.
DR RefSeq; WP_010869937.1; NC_000909.1.
DR AlphaFoldDB; Q57880; -.
DR SMR; Q57880; -.
DR STRING; 243232.MJ_0438; -.
DR PRIDE; Q57880; -.
DR EnsemblBacteria; AAB98426; AAB98426; MJ_0438.
DR GeneID; 1451298; -.
DR KEGG; mja:MJ_0438; -.
DR eggNOG; arCOG00048; Archaea.
DR HOGENOM; CLU_032119_0_0_2; -.
DR InParanoid; Q57880; -.
DR OMA; GFMYKAN; -.
DR OrthoDB; 47556at2157; -.
DR PhylomeDB; Q57880; -.
DR BRENDA; 2.1.1.256; 3260.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016423; F:tRNA (guanine) methyltransferase activity; IDA:UniProtKB.
DR GO; GO:0030488; P:tRNA methylation; IDA:UniProtKB.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR000241; RNA_methylase_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR004114; THUMP_dom.
DR Pfam; PF02926; THUMP; 1.
DR Pfam; PF01170; UPF0020; 1.
DR SMART; SM00981; THUMP; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
DR PROSITE; PS51165; THUMP; 1.
DR PROSITE; PS01261; UPF0020; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Methyltransferase; Reference proteome; RNA-binding;
KW S-adenosyl-L-methionine; Transferase; tRNA processing.
FT CHAIN 1..381
FT /note="tRNA (guanine(6)-N2)-methyltransferase"
FT /id="PRO_0000140480"
FT DOMAIN 43..157
FT /note="THUMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00529"
FT BINDING 173..177
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8U248"
FT BINDING 204..206
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8U248"
FT BINDING 261
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8U248"
FT BINDING 289..290
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8U248"
FT BINDING 306
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250|UniProtKB:Q8U248"
SQ SEQUENCE 381 AA; 43738 MW; 9BB972D94479444D CRC64;
MDYYVTLSPG LEKISKNEIE SFGGKIKEIR ENKGRIFFSG DLKLIPKINY LSRTIERMNI
LLHREEIPNI ALDDIYKRVY NIDWTEWIKE NQSFAIRPLR AGEHNFTSID IGRVAGEAVI
KSYQRDKNIR LKVNLDEPDV IVRVEVIFDE LIVGIDTTGD IALDKRGYRV FNHPAHLNAT
IASSLVYLSD WKDDEMLLDP MCGSGTIPIE GALMKRNIPP GKFRENKYGF KFIDIFGYEL
LDKIKKEIVE NKNIYKIIGL DKNQKYLDGA KDNAKNAEVL DTIEFICGDA TKLHEKFNES
DVIIANPPYG IRIGSKRSVK KLYDEFLSSA KEIMHGSSRL IVITAEDKMF KDAIAKNNFE
VKEEFNVMFG GLMTRVFYLT L
